2R33

Crystal structure of a Bowman-Birk inhibitor from Vigna unguiculata seeds

「2OT6」から置き換えられました

2R33 の概要

• エントリーDOI: 10.2210/pdb2r33/pdb
• 関連するPDBエントリー: 2OT6
• 分子名称: Bowman-Birk type seed trypsin and chymotrypsin inhibitor (2 entities in total)
• 機能のキーワード: bowman-birk protease inhibitor, vigna unguiculata, plant-pis, protein-protein interactions, serine protease inhibitor, plant protein
• 由来する生物種: Vigna unguiculata (cowpea)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16006.12

構造登録者

Rao, K.N.,Suresh, C.G. (登録日: 2007-08-28, 公開日: 2007-11-27, 最終更新日: 2024-11-06)

主引用文献

Rao, K.N.,Suresh, C.G.
Bowman-Birk protease inhibitor from the seeds of Vigna unguiculata forms a highly stable dimeric structure.
Biochim.Biophys.Acta, 1774:1264-1273, 2007

PubMed Abstract: Different protease inhibitors including Bowman-Birk type (BBI) have been reported from the seeds of Vigna unguiculata. Protease isoinhibitors of double-headed Bowman-Birk type from the seeds of Vigna unguiculata have been purified and characterized. The BBI from Vigna unguiculata (Vu-BBI) has been found to undergo self-association to form very stable dimers and more complex oligomers, by size-exclusion chromatography and SDS-PAGE in the presence of urea. Many BBIs have been reported to undergo self-association to form homodimers or more complex oligomers in solution. Only one dimeric crystal structure of a BBI (pea-BBI) is reported to date. We report the three-dimensional structure of a Vu-BBI determined at 2.5 A resolution. Although, the inhibitor has a monomer fold similar to that found in other known structures of Bowman-Birk protease inhibitors, its quaternary structure is different from that commonly observed in this family. The structural elements responsible for the stability of monomer molecule and dimeric association are discussed. The Vu-BBI may use dimeric or higher quaternary association to maintain the physiological state and to execute its biological function.

PubMed: 17869196
DOI: 10.1016/j.bbapap.2007.07.009

実験手法

X-RAY DIFFRACTION (2.5 Å)